CAZyme Information: MGYG000004515_01346

Basic Information

• Species: UMGS1663 sp900753245
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; UMGS1663; UMGS1663 sp900753245
• CAZyme ID: MGYG000004515_01346
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
410	MGYG000004515_23|CGC1	45831.81	6.284

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004515	1468039	MAG	Israel	Asia

• Gene Location: Start: 1872; End: 3104 Strand: -

Full Sequence      

MKNIRKILVSVLIVITMPMYVLIAPVYAFGPSSSNIYEGIDVSGWQGNIDYKQVVNSGIQ
IVYMKASEGTNFVDPYFNQNYSNAKANGLKVGFYHYLTARSVNDAIKQANFFVSTISGKT
PDCRLAMDFESFGNLNREEINEIGLTFMKTVENLSGKKMVIYSDTSNASNVFSGELTNYP
IWVAQYEIQEPTSNGNWNNWIGWQYTDAGKISGINGYVDRDKFTEEILLNESSEIPLPDN
TNKPSAGGTTTIIIQRGDTLSRIAIKYNTTVQRLVELNNIANPNLIYAGNTLIVPSGEVE
SDTDGNSTSGQTIYIVQRGDTLNKIALEFGTTARAIAEENNIRNINLIYVGQRLIIPTHR
YDLNHTLYKIQYGDTLWSISRRYGVPIATIVRLNRIQNPNLIYAGTTIRI

Enzyme Prediction     

No EC number prediction in MGYG000004515_01346.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	40	214	1.5e-52	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	2.75e-78	39	223	2	184	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd00599	GH25_muramidase	1.20e-57	39	223	2	186	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
pfam01183	Glyco_hydro_25	1.31e-56	40	214	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	5.25e-47	36	223	62	253	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06414	GH25_LytC-like	5.94e-45	39	219	3	186	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT55024.1	4.23e-119	28	410	27	408
QJS18123.1	2.73e-118	28	409	24	395
QBE96304.1	1.03e-111	26	410	23	402
QIB56830.1	5.84e-111	26	410	23	402
QMW80393.1	5.84e-111	26	410	23	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	2.35e-55	38	243	21	226	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	7.69e-54	38	243	21	226	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5A6S_A	2.10e-32	31	228	16	206	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	4.40e-26	38	223	6	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	7.81e-23	38	223	17	206	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	7.12e-51	33	228	5	201	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.60e-35	38	318	2	260	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
Q8X7H0	7.01e-32	25	228	53	261	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	1.35e-31	25	223	53	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.35e-31	25	223	53	254	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000293	0.999081	0.000174	0.000164	0.000150	0.000142

TMHMM  Annotations     

start	end
7	29